Carboxylmethylation of the β subunit of xENaC regulates channel activity

Michael D. Rokaw, Jun Min Wang, Robert S. Edinger, Ora A. Weisz, Daniel Hui, Pamela Middleton, Vadim Shlyonsky, Bakhrom K. Berdiev, Iskander Ismailov, Douglas C. Eaton, Dale J. Benos, John P. Johnson

Research output: Contribution to journalArticlepeer-review

50 Citations (Scopus)


The action of aldosterone to increase apical membrane permeability in responsive epithelia is thought to be due to activation of sodium channels. Aldosterone stimulates methylation of a 95-kDa protein in apical membrane of A6 cells, and we have previously shown that methylation of a 95-kDa protein in the immunopurified Na+ channel complex increases open probability of these channels in planar lipid bilayers. We report here that aldosterone stimulates carboxylmethylation of the β subunit of xENaC in A6 cells. In vitro translated β subunit, but not α or γ, serves as a substrate for carboxylmethylation. Carboxylmethylation of ENaC reconstituted in planar lipid bilayers leads to an increase in open probability only when β subunit is present. When the channel complex is immunoprecipitated from A6 cells and analyzed by Western blot with antibodies to the three subunits of xENaC, all three subunits are recognized as constituents of the complex. The results suggest that Na+ channel activity in A6 cells is regulated, in part, by carboxylmethylation of the β subunit of xENaC.

Original languageEnglish
Pages (from-to)28746-28751
Number of pages6
JournalJournal of Biological Chemistry
Issue number44
Publication statusPublished - Oct 30 1998

ASJC Scopus subject areas

  • Biochemistry
  • Molecular Biology
  • Cell Biology

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